Role of the Dc domain of the bacterial hook protein FlgE in hook assembly and function

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Author(s)

    • Moriya Nao
    • Graduate School of Frontier Biosciences, Osaka University
    • Ferris Hedda
    • Department of Molecular Biophysics and Biochemistry, Yale University
    • Morimoto Yusuke V.
    • Graduate School of Frontier Biosciences, Osaka University|Riken Quantitative Biology Center
    • Namba Keiichi
    • Graduate School of Frontier Biosciences, Osaka University|Riken Quantitative Biology Center

Abstract

The bacterial flagellar hook acts as a universal joint to smoothly transmit torque produced by the motor to the filament. The hook protein FlgE assembles into a 55 nm tubular structure with the help of the hook cap (FlgD). FlgE consists of four domains, D0, Dc, D1 and D2, arranged from the inner to the outer part of the tubular structure of the hook. The Dc domain contributes to the structural stability of the hook, but it is unclear how this Dc domain is responsible for the universal joint mechanism. Here, we carried out a deletion analysis of the FlgE Dc domain. FlgEΔ4/5 with deletion of residues 30 to 49 was not secreted into the culture media. FlgEΔ5 and FlgEΔ6 with deletions of residues 40 to 49 and 50 to 59, respectively, still formed hooks, allowing the export apparatus to export the hook-filament junction proteins FlgK and FlgL and flagellin FliC. However, these deletions inhibited the replacement of the FlgD hook cap by FlgK at the hook tip, thereby abolishing filament formation. Deletion of residues 50 to 59 significantly affected hook morphology. These results suggest that the Dc domain is responsible not only for hook assembly but also for FlgE export, the interaction with FlgK, and the polymorphic supercoiling mechanism of the hook.<br>

Journal

  • BIOPHYSICS

    BIOPHYSICS 9(0), 63-72, 2013

    The Biophysical Society of Japan

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